کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1356784 981159 2008 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Protein phosphatase inhibitory activity of tautomycin photoaffinity probes evaluated at femto-molar level
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Protein phosphatase inhibitory activity of tautomycin photoaffinity probes evaluated at femto-molar level
چکیده انگلیسی

Herein we describe the further improvement of our in-house developed firefly bioluminescence assay system for the determination of inhibition of protein phosphatase (PP). The advantage with the new system is higher sensitivity as well as being time and sample efficient. The inhibition activity of tautomycin with PP1γ was determined using the upgraded test system and Ki was found to be 4.5 nM, which compare favorably with the activity reported previously by others using different methods. The test system was then used in order to determine the activity of nine tautomycin (TTM) photoaffinity probes. One of the TTM photoaffinity probes (anti-10) was found to possess higher activity than the natural product itself with a Ki of 3.4 nM, while the remaining photoaffinity probes were found to possess Ki in the range of 8.0–213 nM.

Development of a highly sensitive firefly bioluminescence assay system was, in fact, applied to ten tautomycin analogs having photoaffinity probes to obtain the Ki values in the range of 3.4–213 nM, and one of them showed slightly higher activity than the natural tautomycin diacid derivative.Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry - Volume 16, Issue 4, 15 February 2008, Pages 1747–1755
نویسندگان
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